5LK6

Crystal structure of a lipase carboxylesterase from Sulfolobus islandicus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Collection date	2012-10-31
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 43 21 2
Unit cell lengths	166.410, 166.410, 185.780
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.420 - 2.600
R-factor	0.15892
Rwork	0.157
R-free	0.19430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3aik
RMSD bond length	0.019
RMSD bond angle	2.059
Data reduction software	XDS (September 26, 2012)
Data scaling software	SCALA (3.3.20)
Phasing software	PHASER (2.5.1)
Refinement software	REFMAC (5.8.0155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.420	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.136	0.543
Number of reflections	79041
<I/σ(I)>	5.6	1.4
Completeness [%]	93.3	99.3
Redundancy	10.4	10.62

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	Hampton Reaserch Crystal Screen 2 (HR2-112) Condition #23. 1.6 M Ammonium sulfate, 0.1 M MES monohydrate pH 6.5, 10% v/v 1,4-Dioxane. Reservoir volume 600 uL. 2 uL of EstA 10 mg/mL in 50 mM Tris pH 8, mixed with 2 uL of reservoir volume for hanging drop at room temperature.